WELL-ORDERED CRYSTALS OF A SHORT-CHAIN ALCOHOL-DEHYDROGENASE FROM DROSOPHILA-LEBANONENSIS - RE-EVALAUTION OF THE CRYSTALLOGRAPHIC DATA AND ROTATION FUNCTION-ANALYSIS

Alcohol dehydrogenase prepared from Drosophila lebanonesis yields well ordered plate-like crystals which diffract to better than 2.3 Angstro m resolution. The crystals belong to space group P2(1) of the monoclin ic system; the unit-cell dimensions are a = 65.25, b = 55.77, c = 70.0 2 Angstrom, alpha = 90, beta = 107.08, gamma = 90 degrees. The asymmet ric unit of the crystal cell is most probably occupied by a dimer, cor responding to a packing density of 2.15 Angstrom(3) Da(-1). The orient ation of the noncrystallographic twofold symmetry axes is determined b y analysis of a self-rotation function calculated with native intensit y data.